mutA Family assigned · medium auto-curated

H37Rv Rv1492 · MTBC0 mtbc0_001596 · 615 aa · 1691962–1693809 (+) · RefSeq NP_216008.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)methylmalonyl-CoA mutase small subunit
MTBC0 PGAP re-annotationmethylmalonyl-CoA mutase small subunit
Revised (this work)Methylmalonyl-CoA mutase small subunit. Pfam: MM_CoA_mutase (PF01642.29).

Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.

Curated reference (UniProt)

UniProt P9WJK7 SwissProt · reviewed · Evidence at protein level
UniProt nameProbable methylmalonyl-CoA mutase small subunit
EC (curated) EC 5.4.99.2
Curated functionCatalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Preferred namemutA
eggNOG descriptionMethylmalonyl-CoA mutase
Orthologous groupCOG1884
EC number EC 5.4.99.2
KEGG orthology K01847
KEGG pathways map00280, map00630, map00640, map00720, map01100, map01120, map01200
KEGG modules M00373, M00376, M00741
Gene Ontology (32) GO:0005575, GO:0005618, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0005886, GO:0006082, GO:0006629, GO:0006631, GO:0008150, GO:0008152 +20 more

Orthology-based transfer (eggNOG 5.0.2, diamond). EC/KO/GO/CAZy are computed annotations, not manual curation; cross-check against the primary literature before treating a specific reaction as established.

Conservation & selection (intra-MTBC, 145 209 strains)

pN/pS 0.127 · strong purifying
Polymorphic sites (≥ 0.1% of strains) 6 synonymous, 2 missense, 0 nonsense, 0 frameshift

pN/pS from segregating SNPs (singletons removed) normalised by possible sites. Low pN/pS = purifying selection (a strong signal that a "hypothetical" is a real, constrained gene). A high pN/pS is ambiguous: relaxed constraint or positive selection (drug resistance, antigenic variation) inflate it; e.g. rpoB/katG/pncA score high here for resistance, not loss of function. A clonal disruption (one allele over a clade) suggests lineage pseudogenisation; a convergent one (many independent alleles) is typical of resistance loss-of-function.

Domains (Pfam, hmmscan --cut_ga)

PfamAccessioni-EvalueResiduesDescription
MM_CoA_mutasePF01642.29 1.9e-6249–483 Methylmalonyl-CoA mutase

Functional interaction network (STRING v12, guilt-by-association)

Closest characterised functional partner: mutB (methylmalonyl-CoA mutase large subunit), high confidence from genomic context alone (score 1000 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1493 mutB methylmalonyl-CoA mutase large subunit 999 1000 ctx neighborhood:801 coexpression:784 experimental:999 database:900
Rv1489A hyp hypothetical protein 998 999 coexpression:688 experimental:994
Rv1496 meaB transport system kinase 982 981 ctx neighborhood:867 cooccurence:774 coexpression:404
Rv1322A hyp hypothetical protein 994 974 ctx cooccurence:738 database:900 textmining:818
Rv0951 sucC succinyl-CoA ligase subunit beta 926 905 database:900
Rv0952 sucD succinyl-CoA ligase subunit alpha 919 903 database:900
Rv2495c bkdC branched-chain keto acid dehydrogenase E2 component 830 808 database:800
Rv2215 dlaT pyruvate dehydrogenase E2 component dihydrolipoamide acyltransferase 822 808 database:800
Rv2455c korA 2-oxoglutarate oxidoreductase subunit KorA 885 806 database:800 textmining:432
Rv0889c citA citrate synthase 2 868 806 database:800
Rv2967c pca pyruvate carboxylase 820 805 database:800
Rv2852c mqo malate:quinone oxidoreductase 802 803 database:800
Rv2454c korB 2-oxoglutarate oxidoreductase subunit KorB 848 802 database:800
Rv1240 mdh malate dehydrogenase 835 802 database:800
Rv0896 gltA2 citrate synthase 1 860 801 database:800

STRING combines evidence channels (neighborhood, fusion, cooccurrence, coexpression, experimental, database, text-mining) into a 0–1000 score. The ctx badge marks edges carried by the genomic-context channels (conserved neighborhood, fusion, phylogenetic co-occurrence), which are independent of orthology and structure and the strongest signal for an unknown gene. The no text-mining column recomputes the score from data alone, so a link that does not depend on the literature is visible. Association is a function hypothesis, not proof: corroborate with the operon context and the primary literature before assigning a function.

Evidence

  • Legacy H37Rv annotation: methylmalonyl-CoA mutase small subunit
  • MTBC0 PGAP product: methylmalonyl-CoA mutase small subunit
  • Pfam (hmmscan --cut_ga): MM_CoA_mutase PF01642.29 (E=2e-62)
  • (auto-curated by rules from PGAP + Pfam + Foldseek; not hand-reviewed)

Sources

  • Ancestral sequence & coordinates: Harrison LB et al. (2024), An imputed ancestral reference genome for the MTBC, doi:10.1101/2023.09.07.556366
  • Product annotation: NCBI PGAP on MTBC0; legacy from H37Rv NC_000962.3 (RefSeq NP_216008.1)
  • Domains: Pfam-A via hmmscan --cut_ga — MM_CoA_mutase (PF01642.29)
  • Sequence-level signal: ESM Atlas (EvolutionaryScale × BioHub) — exploratory
  • Controlled vocabulary: eggNOG-mapper 2.1.12 (Cantalapiedra et al. 2021, doi:10.1093/molbev/msab293), eggNOG 5.0 DB (Huerta-Cepas et al. 2019) — OG COG1884
  • Curated reference: UniProt P9WJK7 (SwissProt, reviewed; Evidence at protein level)
  • Intra-MTBC selection: pN/pS and disruption from SPDI variants of 145 209 MTBC strains (this work, local collection vs H37Rv NC_000962.3)
  • Interaction network: STRING v12.0 (Szklarczyk et al. 2023, doi:10.1093/nar/gkac1000), taxon 83332, CC-BY 4.0 — 32 functional partner(s); context anchor mutB
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001596|Rv1492|mutA
MSIDVPERADLEQVRGRWRNAVAGVLSKSNRTDSAQLGDHPERLLDTQTADGFAIRALYTAFDELPEPPLPGQWPFVRGGDPLRDVHSGWKVAEAFPANGATADTNAAVLAALGEGVSALLIRVGESGVAPDRLTALLSGVYLNLAPVILDAGADYRPACDVMLALVAQLDPGQRDTLSIDLGADPLTASLRDRPAPPIEEVVAVASRAAGERGLRAITVDGPAFHNLGATAATELAATVAAAVAYLRVLTESGLVVSDALRQISFRLAADDDQFMTLAKMRALRQLWARVAEVVGDPGGGAAVVHAETSLPMMTQRDPWVNMLRCTLAAFGAGVGGADTVLVHPFDVAIPGGFPGTAAGFARRIARNTQLLLLEESHVGRVLDPAGGSWFVEELTDRLARRAWQRFQAIEARGGFVEAHDFLAGQIAECAARRADDIAHRRLAITGVNEYPNLGEPALPPGDPTSPVRRYAAGFEALRDRSDHHLARTGARPRVLLLPLGPLAEHNIRTTFATNLLASGGIEAIDPGTVDAGTVGNAVADAGSPSVAVICGTDARYRDEVADIVQAARAAGVSRVYLAGPEKALGDAAHRPDEFLTAKINVVQALSNLLTRLGA